Th conformational analysis at the residue level using proton nmr for the following oligopeptide series is in progress: Boc-(Met)n-OMe, Z-(Glu)n-OEt, Boc-(Glu)n-OPOE (where n equals 2-7, Boc equals t-butyloxycarbonyl, Z equals benzyloxycarbonyl, POE equals polyoxyethylene). Assignments for individual N-H and alpha-CH residues have been accomplished for the methionine series up to the heptamer through inclusion of a "guest" amino acid residue for a methionine residue, incorporation of deuterium labelled methionine residues, and homonuclear spin decoupling. Through solvent and temperature dependence of chemical shifts as well as IR analysis, we were able to propose a novel seven membered ring structure for the methionine heptamer in CDCl3. In addition, conformations for lower oligomers of this series have been proposed. Preliminary NMR analysis of both glutamate series show evidence for structural similarities to the methionine homo-oligopeptide series. In an effort to extend these studies to higher oligomers of the glutamate series, we have attached the peptides to polyoxyethylene to enhance their solubility. High resolution proton NMR spectra have been obtained for these POE bound peptides up to the hexamer.